Abstract
Using data obtained from 1H-1H correlated spectroscopy and one- and two-dimensional NOE measurements, we have determined the preferential solution conformation of the disaccharide unit Galβ(1-3)Gal-NAc in the antifreeze glycopeptide (Galß(l-3)GalNAcαl-Thr-Ala-Ala)n derived from the blood of the antarctic fish Trematomas borchgrevinki. The disaccharide, which is a rigid unit, exists with a restricted orientation about the GalNAc-αl-Thr linkage. Preliminary evidence indicates that the backbone (Ala-Ala-Thr)n lies in an extended helical conformation. Antifreeze glycopeptide 1H NMR Glycosidic linkage Dissaccharide structure Nuclear Overhauser effect.
Original language | English (US) |
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Pages (from-to) | 133-137 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 183 |
Issue number | 1 |
DOIs | |
State | Published - Apr 8 1985 |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology